Crystallization and diffraction analysis of beta-N-acetylhexosaminidase from Aspergillus oryzae
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F11%3A10100473" target="_blank" >RIV/00216208:11310/11:10100473 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/11:00370659 RIV/68378050:_____/11:00370659 RIV/61388963:_____/11:00370659
Result on the web
<a href="http://dx.doi.org/10.1107/S1744309111004945" target="_blank" >http://dx.doi.org/10.1107/S1744309111004945</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1107/S1744309111004945" target="_blank" >10.1107/S1744309111004945</a>
Alternative languages
Result language
angličtina
Original language name
Crystallization and diffraction analysis of beta-N-acetylhexosaminidase from Aspergillus oryzae
Original language description
Fungal beta-N-acetylhexosaminidases are enzymes that are used in the chemoenzymatic synthesis of biologically interesting oligosaccharides. The enzyme from Aspergillus oryzae was produced and purified from its natural source and crystallized using the hanging-drop vapour-diffusion method. Diffraction data from two crystal forms (primitive monoclinic and primitive tetragonal) were collected to resolutions of 3.2 and 2.4 A, respectively. Electrophoretic and quantitative N-terminal protein-sequencing analyses confirmed that the crystals are formed by a complete biologically active enzyme consisting of a glycosylated catalytic unit and a noncovalently attached propeptide.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
<a href="/en/project/1M0505" target="_blank" >1M0505: Center of targeted therapeutic drugs</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2011
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
ISSN
1744-3091
e-ISSN
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Volume of the periodical
67
Issue of the periodical within the volume
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Country of publishing house
GB - UNITED KINGDOM
Number of pages
6
Pages from-to
498-503
UT code for WoS article
000289738400020
EID of the result in the Scopus database
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